Full-text resources of PSJD and other databases are now available in the new Library of Science.
Visit https://bibliotekanauki.pl


Preferences help
enabled [disable] Abstract
Number of results


2013 | 8 | 3 | 297-301

Article title

Vimentin cleavage in end-stage renal disease is not related to apoptosis


Title variants

Languages of publication



Anti-vimentin auto-antibodies contribute to chronic allograft nephropathy. They exist in sera of end-stage renal disease patients on hemodialysis (ESRD) already before renal transplantation. We found recently that a 49 kDa vimentin fragment is increased in lymphocytes of ESRD patients which is presented on the cell surface. In vitro studies showed that such a fragment is formed during apoptosis by active caspase-3. We hypothesized that vimentin degradation in leukocytes of ESRD patients correlates to caspase-3 activation in vivo. Lymphocytes and monocytes were isolated from ESRD patients and from healthy volunteers and analyzed for vimentin expression and caspase-3 activation. In addition, apoptosis was induced in vitro and quantified by flow cytometry. ESRD monocytes have shown only the full length 60 kDa vimentin isoform. ESRD lymphocytes, however, showed in addition a strongly increased expression of the 49 kDa vimentin in all samples. Caspase-3 activation was found in 60% of ESRD lymphocytes and 66% of ESRD monocytes but not in healthy volunteers. UV-mediated induction of apoptosis was not associated with vimentin degradation. These experiments could confirm increased vimentin degradation in ESRD lymphocytes. However, we could not validate any correlation to apoptosis.










Physical description


1 - 6 - 2013
17 - 4 - 2013


  • Department of Surgery, Medical University of Vienna, A-1090, Vienna, Austria
  • Department of Surgery, Medical University of Vienna, A-1090, Vienna, Austria
  • Department of Surgery, Medical University of Vienna, A-1090, Vienna, Austria
  • Department of Internal Medicine-I, Medical University of Vienna, A-1090, Vienna, Austria
  • Department of Internal Medicine-I, Medical University of Vienna, A-1090, Vienna, Austria
  • Department of Surgery, Medical University of Vienna, A-1090, Vienna, Austria


  • [1] Minin AA, Moldaver MV, Intermediate vimentin filaments and their role in intracellular organelle distribution, Biochemistry (Mosc), 2008, 73, 1453–1466 http://dx.doi.org/10.1134/S0006297908130063[Crossref][WoS]
  • [2] Jurcevic S, Ainsworth ME, Pomerance A, Smith JD, Robinson DR, Dunn MJ, et al., Antivimentin antibodies are an independent predictor of transplant-associated coronary artery disease after cardiac transplantation, Transplantation, 2001, 71, 886–892 http://dx.doi.org/10.1097/00007890-200104150-00011[Crossref]
  • [3] Jonker M, Danskine A, Haanstra K, Wubben J, Kondova I, Kuhn EM, et al., The autoimmune response to vimentin after renal transplantation in nonhuman primates is immunosuppression dependent, Transplantation, 2005, 80, 385–393 http://dx.doi.org/10.1097/01.tp.0000166920.18998.15[Crossref]
  • [4] Barber LD, Whitelegg A, Madrigal JA, Banner NR, Rose ML, Detection of vimentin-specific autoreactive CD8+ T cells in cardiac transplant patients, Transplantation, 2004, 77, 1604–1609 http://dx.doi.org/10.1097/01.TP.0000129068.03900.25[Crossref]
  • [5] Bilalic S, Veitinger M, Ahrer KH, Gruber V, Zellner M, Brostjan C, et al., Identification of Non-HLA antigens targeted by alloreactive antibodies in patients undergoing chronic hemodialysis, J Proteome Res, 2010, 9, 1041–1049 http://dx.doi.org/10.1021/pr900930d[Crossref][WoS]
  • [6] Moisan E, Girard D, Cell surface expression of intermediate filament proteins vimentin and lamin B1 in human neutrophil spontaneous apoptosis, J Leukoc Biol, 2006, 79, 489–498 http://dx.doi.org/10.1189/jlb.0405190[Crossref]
  • [7] Mor-Vaknin N, Punturieri A, Sitwala K, Markovitz DM, Vimentin is secreted by activated macrophages, Nat Cell Biol, 2003, 5, 59–63 http://dx.doi.org/10.1038/ncb898[Crossref]
  • [8] Bilalic S, Michlmayr A, Gruber V, Buchberger E, Burghuber C, Bohmig GA, et al., Lymphocyte activation induces cell surface expression of an immunogenic vimentin isoform, Transplant immunology, 2012 [WoS][Crossref]
  • [9] He B, Lu N, Zhou Z, Cellular and nuclear degradation during apoptosis, Curr Opin Cell Biol, 2009, 21, 900–912 http://dx.doi.org/10.1016/j.ceb.2009.08.008[Crossref][WoS]
  • [10] Kuranaga E, Beyond apoptosis: caspase regulatory mechanisms and functions in vivo, Genes Cells, 2012 [Crossref][WoS]
  • [11] Kumar S, Caspase function in programmed cell death, Cell Death Differ, 2007, 14, 32–43 http://dx.doi.org/10.1038/sj.cdd.4402060[Crossref]
  • [12] Byun Y, Chen F, Chang R, Trivedi M, Green KJ, Cryns VL, Caspase cleavage of vimentin disrupts intermediate filaments and promotes apoptosis, Cell Death Differ, 2001, 8, 443–450 http://dx.doi.org/10.1038/sj.cdd.4400840[Crossref]
  • [13] Bhaskaran M, Ranjan R, Shah H, Siu J, Colvin R, Radhakrishnan N, et al., Lymphopenia in dialysis patients: a preliminary study indicating a possible role of apoptosis, Clin Nephrol, 2002, 57, 221–229 http://dx.doi.org/10.5414/CNP57221[Crossref]
  • [14] Borges A, Borges M, Fernandes J, Nascimento H, Sameiro-Faria M, Miranda V, et al., Apoptosis of Peripheral CD4(+) T-Lymphocytes in End-Stage Renal Disease Patients Under Hemodialysis and rhEPO Therapies, Renal Failure, 2011, 33, 138–143 http://dx.doi.org/10.3109/0886022X.2011.553300[WoS][Crossref]
  • [15] Guo LL, Pan Y, Zhu XJ, Tan LY, Xu QJ, Jin HM, Conventional, but not high-purity, dialysate-induced monocyte apoptosis is mediated by activation of PKC-delta and inflammatory factors release, Nephrol Dial Transplant, 2011, 26, 1516–1522 http://dx.doi.org/10.1093/ndt/gfq620[Crossref]
  • [16] Pahl MV, Gollapudi S, Sepassi L, Gollapudi P, Elahimehr R, Vaziri ND, Effect of end-stage renal disease on B-lymphocyte subpopulations, IL-7, BAFF and BAFF receptor expression, Nephrol Dial Transplant, 2010, 25, 205–212 http://dx.doi.org/10.1093/ndt/gfp397[Crossref]
  • [17] Andreoli MC, Dalboni MA, Watanabe R, Manfredi SR, Canziani ME, Kallas EG, et al., Impact of dialyzer membrane on apoptosis and function of polymorphonuclear cells and cytokine synthesis by peripheral blood mononuclear cells in hemodialysis patients, Artif Organs, 2007, 31, 887–892 http://dx.doi.org/10.1111/j.1525-1594.2007.00485.x[WoS][Crossref]
  • [18] Pernice F, Floccari F, Nostro L, Caccamo C, Belghity N, Mantuano S, et al., Oxidative stress, sister chromatid exchanges and apoptosis in the pathogenesis of lymphocytopenia in ESRD patients, J Nephrol, 2006, 19, 613–620
  • [19] Meier P, Spertini F, Blanc E, Burnier M, Oxidized low-density lipoproteins activate CD4+ T cell apoptosis in patients with end-stage renal disease through Fas engagement, J Am Soc Nephrol, 2007, 18, 331–342 http://dx.doi.org/10.1681/ASN.2006050514[Crossref][WoS]
  • [20] Cohen G, Raupachova J, Wimmer T, Deicher R, Horl WH, The uraemic retention solute parahydroxy-hippuric acid attenuates apoptosis of polymorphonuclear leukocytes from healthy subjects but not from haemodialysis patients, Nephrol Dial Transplant, 2008, 23, 2512–2519 http://dx.doi.org/10.1093/ndt/gfn098[WoS][Crossref]
  • [21] Ranjan R, Shah H, Siu J, Varghese E, Bhaskaran M, Reddy K, et al., Monocyte apoptosis in dialysis patients is Fas ligand-mediated, Clin Nephrol, 2002, 58, 423–430 http://dx.doi.org/10.5414/CNP58423[Crossref]

Document Type

Publication order reference


YADDA identifier

JavaScript is turned off in your web browser. Turn it on to take full advantage of this site, then refresh the page.